Physico-chemical factors controlling the foamability and foam stability of milk proteins: Sodium caseinate and whey protein concentrates

Marinova, K. P.; Basheva, Elka S.; Nenova, Boriana; Temelska, M.I.; Mirarefi, Amir Y.; Campbell, Bruce; Ivanov, Ivan B.

doi:10.1016/j.foodhyd.2009.03.003

Cited by 217 publications

(156 citation statements)

References 40 publications

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“…1b). This result was in agreement with previous reports which mentioned that the faster adsorption kinetics is related to better foam forming capacity of protein solutions [19][20][21]. However, Rouimi et al [22] reported that values of equilibrium surface tension (γ e ) are linked to the foam formation but are not the only criteria.…”

Section: Effect Of Date Palm Sex On the Surface Tension Of Dpssupporting

confidence: 92%

Foamability and Foam Stability of Male and Female Date Palm Sap (Phoenix dactylifera L.) During the Collection Period

et al. 2015

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This work aimed to study the influence of date palm sex on the surface properties of date palm sap (DPS) (Phoenix dactylifera L.) during the collection period. The behavior at the interface and foaming properties were evaluated via equilibrium surface tension (drop volume) and bubbling method, respectively. Unlike male sap, the female sap was unable to produce foam due to its low rate of adsorption, low average hydrophobicity values, and low bulk viscosity values throughout the collection period. For male sap, there are significant differences (p<0.05) on foaming properties throughout the collection period. In fact, the last 3 weeks of sap collection were characterized by a decrease pace of surface tension which explains the enhancement of both foam capacity and stability. The last week of collection period present the best foam power (0.9). To explain these differences, the interactions of several factors and their affects on foaming properties were examined. Results showed a positive correlation between foam capacity and average hydrophobicity values. In the other hand, foam stability exhibits a positive correlation with the increase of protein concentration and bulk viscosity.

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Section: Effect Of Date Palm Sex On the Surface Tension Of Dpssupporting

confidence: 92%

Foamability and Foam Stability of Male and Female Date Palm Sap (Phoenix dactylifera L.) During the Collection Period

et al. 2015

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“…The ability of a protein to form a thin film is enhanced by the unfolded structure rather than a globular compact structure (Marinova et al, 2009).…”

Section: Air/water Foamsmentioning

confidence: 99%

Canola/rapeseed protein-functionality and nutrition

Wanasundara¹,

McIntosh²,

Perera³

et al. 2016

OCL

142

103

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-Protein rich meal is a valuable co-product of canola/rapeseed oil extraction. Seed storage proteins that include cruciferin (11S) and napin (2S) dominate the protein complement of canola while oleosins, lipid transfer proteins and other minor proteins of non-storage nature are also found. Although oil-free canola meal contains 36-40% protein on a dry weight basis, non-protein components including fibre, polymeric phenolics, phytates and sinapine, etc. of the seed coat and cellular components make protein less suitable for food use. Separation of canola protein from non-protein components is a technical challenge but necessary to obtain full nutritional and functional potential of protein. Process conditions of raw material and protein preparation are critical of nutritional and functional value of the final protein product. The storage proteins of canola can satisfy many nutritional and functional requirements for food applications. Protein macromolecules of canola also provide functionalities required in applications beyond edible uses; there exists substantial potential as a source of plant protein and a renewable biopolymer. Available information at present is mostly based on the protein products that can be obtained as mixtures of storage protein types and other chemical constituents of the seed; therefore, full potential of canola storage proteins is yet to be revealed.Keywords: Canola / rapeseed storage proteins / cruciferin / napin / protein digestibility / functional properties Résumé -Protéines de canola et de colza : fonctionnalités et nutrition. Les tourteaux riches en protéines repré-sentent un coproduit de valeur de l'extraction de l'huile de canola/colza. Dans la graine, les protéines de stockage, notamment la cruciférine (11S) et la napine (2S), dominent la fraction protéique du canola, mais des oléosines, des protéines de transfert de lipides et d'autres protéines mineures non dédiées au stockage sont également présentes. Bien que le tourteau de canola déshuilé contienne 36-40 % de protéines sur poids sec, la présence de composants non protéiques, dont les fibres, les polymères phénoliques, les phytates, la sinapine, etc. issus de l'enveloppe de la graine et des composants cellulaires rendent les protéines moins appropriées à une utilisation en alimentation humaine. Cette revue présente les connaissances actuelles en termes de valeur nutritionnelle et fonctionnelle des protéines issues des graines de canola. La séparation des protéines de canola des composants non protéiques représente un défi technique mais nécessaire pour libérer totalement le potentiel nutritionnel et fonctionnel de la protéine. Les protéines de stockage de canola peuvent satisfaire un grand nombre d'exigences nutritionnelles et fonctionnelles pour des applications alimentaires. Les macromolécules protéiques de canola offrent également des fonctionnalités requises dans les applications dépassant les seules utilisations alimentaires ; un potentiel important existe en tant que source de protéines végétales et de biopol...

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“…The DST values of 0.13% NaCas ranged from 54.23±1.13 to 53.38±0.68 mN/m during 10 s, which agrees well with the previously reported value of 54 mN/m (for 0.1% NaCas) at the same time frame. 21 When NaCas was added to sucrose solutions, the DST values reduced almost to minimum immediately after the start of the experiment (51.17±0.59 mN/m). This result suggests that sugar molecules do not seem to hinder the movement of the proteins at this level of protein concentration.…”

Section: Dst and Extent Of Protein And Surfactant Migration To The Sumentioning

confidence: 91%

The Effect of Food-Grade Low-Molecular-Weight Surfactants and Sodium Caseinate on Spray Drying of Sugar-Rich Foods

Jayasundera

Adhikari

et al. 2010

Food Biophysics

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The effect of low-molecular-weight surfactants (LMS) and sodium caseinate (NaCas) on spray drying of sugar-rich foods has been studied. Sucrose and NaCas were selected as a model sugar-rich food and protein, respectively. Sodium stearoyl lactylate (SSL) and Polysorbate 80 (Tween 80) were chosen as model ionic and nonionic LMS. SucroseNaCas solutions with the solids ratio of 99.5:0.5 in the absence and presence (0.01% and 0.05%) of SSL and Tween 80 were prepared. The feed solutions had 25% solid concentration in all cases. The dynamic surface tension (DST) values of the solutions were measured for 100 s and the solutions were subsequently spray dried at inlet and outlet temperatures of 165 and 65°C, respectively. The glass-rubber temperature (T g-r ), the surface elemental composition and amorphous-crystalline nature of the powders were also determined. At these concentrations and experimental time frame, it was found that the proteins preferentially migrated to the air-water interface reasonably swiftly. The addition of LMS resulted in partial or complete displacement of the proteins from the air-water interface. For spray-drying trials with the yield of 82.0%, it was found that 52.0% of the powder particle surface was covered with proteins. The powder recovery was greatly reduced by the LMS concentration and type. At 0.05% on dry solid basis, in the case of nonionic surfactant (Tween 80), the displacement of protein from the surface was such that no powder was recovered. The ionic surfactant (SSL) displaced 2.0% and 29.3% proteins from the droplet surface at concentrations of 0.01% and 0.05%, respectively, resulting in 75.5±1.8% and 30.1±1.4% powder yield. The T g-r results revealed that the amount of protein required for successful spray drying of the sucrose-protein solution depends on the amount of proteins present in the droplet surface but not in the bulk. X-ray diffraction and scanning electron microscopy results confirmed that the powders of both sucrose-NaCas and sucrose-NaCas with 0.01% SSL were mostly amorphous, while those with sucrose-NaCas-Tween 80 (0.01%) and sucrose-NaCas-SSL (0.05%) were crystalline.

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Physico-chemical factors controlling the foamability and foam stability of milk proteins: Sodium caseinate and whey protein concentrates

Cited by 217 publications

References 40 publications

Foamability and Foam Stability of Male and Female Date Palm Sap (Phoenix dactylifera L.) During the Collection Period

Foamability and Foam Stability of Male and Female Date Palm Sap (Phoenix dactylifera L.) During the Collection Period

Canola/rapeseed protein-functionality and nutrition

The Effect of Food-Grade Low-Molecular-Weight Surfactants and Sodium Caseinate on Spray Drying of Sugar-Rich Foods

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